protein

Recombinant Human Cytochrome b-245 heavy chain

MBS963114

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Cytochrome b-245 heavy chain

Cytochrome b-245

CGD91-phox; Cytochrome b(558) subunit beta; Cytochrome b558 subunit beta; Heme-binding membrane glycoprotein gp91phox; NADPH oxidase 2; Neutrophil cytochrome b 91 kDa polypeptide; Superoxide-generating NADPH oxidase heavy chain subunit; gp91-1gp91-phoxp22 phagocyte B-cytochrome

cytochrome b-245 heavy chain; Cytochrome b-245 heavy chain; cytochrome b-245, beta polypeptide; CGD91-phox; Cytochrome b(558) subunit beta; Cytochrome b558 subunit beta; Heme-binding membrane glycoprotein gp91phox; NADPH oxidase 2; Neutrophil cytochrome b 91 kDa polypeptide; Superoxide-generating NADPH oxidase heavy chain subunit; gp91-1; gp91-phox; p22 phagocyte B-cytochrome

CYBB

CYBB; CYBB; CGD; NOX2; IMD34; AMCBX2; GP91-1; GP91PHOX; p91-PHOX; GP91-PHOX; NOX2; Cytochrome b558 subunit beta

CY24B_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

283-570

570

ERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEV
GQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGD
WTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVF
SYEVVMLVGAGIGVTPFASILKSVWYKYCNNATNLKLKK
IYFYWLCRDTHAFEWFADLLQLLESQMQERNNAGFLSYN
IYLTGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNW
DNEFKTIASQHPNTRIGVFLC

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Cancer

Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H+ currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.

Cloning the gene for an inherited human disorder -- chronic granulomatous disease -- on the basis of its chromosomal location.Royer-Pokora B., Kunkel L.M., Monaco A.P., Goff S.C., Newburger P.E., Baehner R.L., Cole F.S., Curnutte J.T., Orkin S.H.Nature 322:32-38(1986) CYBB mutation analysis in X-linked chronic granulomatous disease.Jirapongsananuruk O., Niemela J.E., Malech H.L., Fleisher T.A.Clin. Immunol. 104:73-76(2002) NHLBI resequencing and genotyping service (RS&G) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004)

6996021

NP_000388.2

NM_000397.3

P04839

49.21kD

AGE-RAGE Signaling Pathway In Diabetic Complications (1319988); AGE-RAGE Signaling Pathway In Diabetic Complications (1319775); Adaptive Immune System Pathway (1269171); Antigen Processing-Cross Presentation Pathway (1269195); Class I MHC Mediated Antigen Processing Presentation Pathway (1269192); Cross-presentation Of Particulate Exogenous Antigens (phagosomes) Pathway (1269196); HIF-1 Signaling Pathway (695200); Immune System Pathway (1269170); Leukocyte Transendothelial Migration Pathway (83083); Leukocyte Transendothelial Migration Pathway (494)

Cytochrome b (-245) is composed of cytochrome b alpha (CYBA) and beta (CYBB) chain. It has been proposed as a primary component of the microbicidal oxidase system of phagocytes. CYBB deficiency is one of five described biochemical defects associated with chronic granulomatous disease (CGD). In this disorder, there is decreased activity of phagocyte NADPH oxidase; neutrophils are able to phagocytize bacteria but cannot kill them in the phagocytic vacuoles. The cause of the killing defect is an inability to increase the cell's respir

CYBB: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc. Defects in CYBB are a cause of granulomatous disease,chronic, X-linked (CGD). A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life- threatening bacterial/fungal infections. Defects in CYBB are a cause of mycobacteriosis atypical X-linked type 2 (AMCBX2). A rare condition characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine and environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections. Protein type: Membrane protein, multi-pass; Oxidoreductase; Membrane protein, integral; Mitochondrial; EC 1.-.-.-. Chromosomal Location of Human Ortholog: Xp21.1. Cellular Component: integral to plasma membrane; mitochondrion; NADPH oxidase complex; phagocytic vesicle membrane; plasma membrane. Molecular Function: electron carrier activity; FAD binding; heme binding; metal ion binding; protein binding; protein heterodimerization activity; superoxide-generating NADPH oxidase activity; voltage-gated ion channel activity. Biological Process: antigen processing and presentation of exogenous peptide antigen via MHC class I; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; antigen processing and presentation of peptide antigen via MHC class I; cell redox homeostasis; hydrogen peroxide biosynthetic process; inflammatory response; innate immune response; ion transport; respiratory burst; small GTPase mediated signal transduction; superoxide metabolic process; superoxide release; vascular endothelial growth factor receptor signaling pathway. Disease: Granulomatous Disease, Chronic, X-linked; Immunodeficiency 34

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180

1 mg (Yeast)

1835